Abstract
Squalene synthase (EC 2.5.1.21) known as a membrane-bound enzyme condenses two molecules of farnesyl diphosphate (FPP) in a stable intermediate, the presqualene diphosphate (PS) which is then reduced by NAD(P)H to form squalene (S). In spite of various hypotheses concerning the binding sites and reaction centers, the catalytic machinery for the two reactions and the mechanism(s) responsible for the sterol mediated regulation of squalene synthase (SQS), have not been elucidated. Sterol auxotrophic mutant strains (1) can be used as tools for such studies. Therefore, before going to purify SQS from plant sources (2), we have undertaken the purification and comparative characterization of squalene synthase (SQS) from three yeast strains: the wild-type FL100, the mutant strain erg10B and the recombinant strain FK5188 pMF13.
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